Ion exchange chromatography is widely used for protein purification due to several advantages including high speed and low cost. However, this method is not useful for purification of human rhinovirus 3C protease (HRV3C) and tobacco etch virus protease (TEVp) since they do not bind to both cation and anion exchange resins at physiological salt concentrations. Here we report a time- and cost-effective method for the purification of HRV3C and TEVp which ensures high purity and yield. The method entails fusion of 7Lys-tagged maltose-binding protein and 6His-tag to the N- and C-termini of two proteases, respectively, and leads to purification of highly pure protein using Ni-affinity and cation exchange chromatographies in less than 8 hours.
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